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      저자 : 김유삼 ( Young Yil Bahk (검색결과 2 건)
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      • Acidic Isocitrate Lyase from Acinetobacter calcoaceticus Grown on Malonate

        박영일,김유삼,Bahk, Young-Yil,Kim, Yu-Sam Korean Society for Biochemistry and Molecular Biol 1987 한국생화학회지 Vol.20 No.2

        말론산을 유일한 탄소원으로하여 자란 Acinetobacter calcoaceticus에서 일종의 산성 이소시트르산 분해효소가 유도되었다. 이 효소를 황산암모니움분별침전, 옥살산 아가로오스 크로마토그래피, DEAE-Sephacel 음이온 교환, Sephadex G-150 겔거르기, 이타콘산 아가로오스 크로마토 그래파를 통하여 정제하였다. 이 효소 분자는 64, 000 달톤 소단위가 두개로 구성되어 있으며 최적 pH는 6.0이었다. 이소시트르산에 대한 $K_M$은 $8.3{\times}10^{-5}M$이였다. 이 효소의 활성은 숙신산과 이타콘산에 의해서 무경쟁적으로, 옥살산과 글리콜산에 의해서 경쟁적으로 방해를 받았다. 이 효소는 또한 N-에칠말레이미드, P-클로로머큐리페니설폰산, 요드아세트아미드에 의해서 강력하게 방해를 받는 것으로 보아 활성자리에 -SH기가 존재하는 것으로 추정된다. 또 디에칠피로카본산이 이 효소 활성을 방해하는 것으로 보아 활성자리에 이미다졸기가 있음으로 예상된다. An acidic isocitrate lyase was induced in Acinetobacter calcoaceticus grown on malonate as a sole source of carbon. This enzyme was purified 30 fold by the combined methods of ammonium sulfate fractionation, oxalate $\omega$-aminohexyl agarose chromatography, DEAE-Sephacel anion exchange chromatography, Sephadex G-150 gel filtration and itaconate $\omega$-aminohexyl agarose chromatography in an electrophoretically homogeneous form. Molecular size of the enzyme was estimated by Sepharose 6B gel filtration to be 129,000 dalton composed of two 64,000 dalton subunits. The optimum pH for this enzyme was 6.1 and the optimum temperature was about $40^{\circ}C$. The enzyme showed a typical Michaelis-Menten kinetics for the substrate, isocitrate, from which Km was calculated to be $8.3{\times}10^{-5}M$. The enzyme activity was inhibited uncompetitively by succinate and itaconate, and competitively by oxalate and glycolate, respectively. The enzyme activity was also inhibited strongly by N-ethylmaleimide, p-chloromercuripheny-lsulfonic acid and iodoacetamide, suggesting that the enzyme has an active -SH group on or near the active site. And diethylpyrocarbonate was also an inhibitor for the enzyme activity, indicating the possible involvement of imidazole group. The purified enzyme was immunogenic in rat. The antiserum prepared against the enzyme inhibited the enzyme activity more than eighty percent.

      • SCIESCOPUSKCI등재

        말론산에서 자란 Acinetobacter calcoaceticus 의 산성 이소시트르산 분해효소

        박영일,김유삼 ( Young Yil Bahk,Yu Sam Kim ) 생화학분자생물학회 1987 BMB Reports Vol.20 No.2

        An acidic isocitrate lyase was induced in Acinetobacter calcoaceticus grown on malonate as a sole source of carbon. This enzyme was purified 30 fold by the combined methods of ammonium sulfate fractionation, oxalate ω-aminohexyl agarose chromatography, DEAE-Sephacel anion exchange chromatography, Sephadex G-150 gel filtration and itaconate ω-aminohexyl agarose chromatography in an electrophoretically homogeneous form. Molecular size of the enzyme was estimated by Sepharose 6B gel filtration to be 129,000 dalton composed of two 64,000 dalton subunits. The optimum pH for this enzyme was 6.1 and the optimum temperature was about 40℃. The enzyme showed a typical Michaelis-Menten kinetics for the substrate, isocitrate, from which Km was calculated to be 8.3 × 10^-5 M. The enzyme activity was inhibited uncompetitively by succinate and itaconate, and competitively by oxalate and glycolate, respectively. The enzyme activity was also inhibited strongly by N-ethylmaleimide, p-chloromercuripheny-lsulfonic acid and iodoacetamide, suggesting that the enzyme has an active -SH group on or near the active site. And diethylpyrocarbonate was also an inhibitor for the enzyme activity, indicating the possible involvement of imidazole group. The purified enzyme was immunogenic in rat. The antiserum prepared against the enzyme inhibited the enzyme activity more than eighty percent.

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